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Database: UniProt
Entry: A0A0S8FIG2_9GAMM
LinkDB: A0A0S8FIG2_9GAMM
Original site: A0A0S8FIG2_9GAMM 
ID   A0A0S8FIG2_9GAMM        Unreviewed;       480 AA.
AC   A0A0S8FIG2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Aldehyde dehydrogenase {ECO:0000256|PIRNR:PIRNR036492};
GN   ORFNames=AMJ59_06440 {ECO:0000313|EMBL:KPK60496.1};
OS   Gammaproteobacteria bacterium SG8_31.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1703405 {ECO:0000313|EMBL:KPK60496.1, ECO:0000313|Proteomes:UP000051321};
RN   [1] {ECO:0000313|EMBL:KPK60496.1, ECO:0000313|Proteomes:UP000051321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG8_31 {ECO:0000313|EMBL:KPK60496.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT   among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(2015).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009986, ECO:0000256|PIRNR:PIRNR036492,
CC       ECO:0000256|RuleBase:RU003345}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPK60496.1}.
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DR   EMBL; LJTI01000007; KPK60496.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S8FIG2; -.
DR   PATRIC; fig|1703405.3.peg.4781; -.
DR   Proteomes; UP000051321; Unassembled WGS sequence.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   CDD; cd07133; ALDH_CALDH_CalB; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43570:SF16; ALDEHYDE DEHYDROGENASE TYPE III, ISOFORM Q; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR036492}.
FT   DOMAIN          35..450
FT                   /note="Aldehyde dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF00171"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        257
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036492-1"
SQ   SEQUENCE   480 AA;  53347 MW;  F8CD215FD660BE84 CRC64;
     MAASPEFLSE AREIQRMEGI FRAQKEDFAR DPMPSAEARR GHLDQLREGL VARKEQLADA
     LQADFSGRSR HETYAELLAS IQGIRYARSH VRRWMRPSRR RAGLLLATTS CRVYYQPKGV
     VGIMVPFNYP IALSIGPLTC ALAAGNRVML RITESIPNTG LVLKELLGSV FPPERVGVTL
     GLVETSKAFS RLPFDHLLFT GSTETGRQVM RAAADNLTPV TLELGGKSPT LIGEDVPMAM
     AAERICFGKA LNAGQTCVAP DYVLCPASRV DEFVGAFRAA FERMYPDLHR NEDYTSIISD
     AHYRRLQGYL DEARTAGAEV IELNPGGHEG PSATSRKMPV YLLKNVNPGM KVMREEIFGP
     ILPIVTYRTL DEAITYINER PRPLAINLFE NDAERRRHVF DGTHSGGICV NDAITHFIAE
     DLPFGGVGDS GMGHYHAREG FLTFSHHKAV LSRPRVNTAK VLYAPHGGWL QNLLYRIFLR
//
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